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Reviewed, UniProtKB/Swiss-Prot A2CBQ3 (MTNC_PROM3)

Last modified November 3, 2009. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Enolase-phosphatase E1
    EC=3.1.3.77
Alternative name(s):
    2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Gene names
Name: mtnC
Ordered Locus Names: P9303_21781
OrganismProchlorococcus marinus (strain MIT 9303) [Complete proteome] [HAMAP]
Taxonomic identifier59922 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) By similarity.

Catalytic activity

5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate. HAMAP MF_01681

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6. HAMAP MF_01681

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. MasA/mtnC family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Enolase-phosphatase E1 HAMAP MF_01681
PRO_0000357385

Sequences

Sequence LengthMass (Da)Tools
A2CBQ3-1 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 4C79FD589E3C4E5E

FASTA24027,352
        10         20         30         40         50         60 
MLDIEGTTCP TSFVSDTLYP YAYSHLEGFL NEHRENNEIQ SLIDEAWREW QADTDASSKD 

        70         80         90        100        110        120 
LLSKALRKNS SEIVNICSYL HHLITIDRKS SALKDLQGRI WREGYEKGDL CSSLYPETIE 

       130        140        150        160        170        180 
ALRKLKQQDY VLAVYSSGSI SAQKLLYRHT ADGDQTALFS HWFDTRTGNK KESRSYSDIS 

       190        200        210        220        230        240 
IAMNIPVEKV LFVSDSYAEC NAAEKSGMSV LFSLREGNPE QDPHDHKAIK ELCCLFDYLL 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000554 Genomic DNA. Translation: ABM78913.1.
RefSeqYP_001018178.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA2CBQ3.

Genome annotation databases

GeneID4777614.
GenomeReviewsGene locus P9303_21781 in contig CP000554_GR.
KEGGpmf:P9303_21781.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMATTDLNFI.

Family and domain databases

HAMAPMF_01681.
[Tree]
InterProIPR005834. Dehalogen-like_hydro.
IPR010041. Enolase_ppase.
[Graphical view]
PANTHERPTHR20371. Enolase_ppase. 1 hit.
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01691. enolase-ppase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNC_PROM3
AccessionPrimary (citable) accession number: A2CBQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: February 20, 2007
Last modified: November 3, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents